ArticleMicrobial cell factories2011
The acid-tolerant L-arabinose isomerase from the mesophilic Shewanella sp. ANA-3 is highly active at low temperatures.
Article in Microbial cell factories, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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9 citing papers in PubMed, 35 citations in OpenAlex.
- Discovery and Preliminary Characterization of Lactose-Transforming Enzymes inInternational journal of molecular sciences · 2026Article
- Comparison of Two l-Arabinose Isomerases for Multienzymatic Conversion of Lactose in Skim Milk Permeate at Neutral and Acidic pH.Journal of agricultural and food chemistry · 2025Article
- Development and Characterization of a Tunable Metal-Organic Framework (MOF) for the Synthesis of a Rare Sugar D-Tagatose.Applied biochemistry and biotechnology · 2025Article
- Efficient D-allulose synthesis under acidic conditions by auto-inducing expression of the tandem D-allulose 3-epimerase genes in Bacillus subtilis.Microbial cell factories · 2022Article
- Biochemical Characterization of Heat-Tolerant Recombinant L-Arabinose Isomerase from Enterococcus faecium DBFIQ E36 Strain with Feasible Applications in D-Tagatose Production.Molecular biotechnology · 2019Article
- Engineering the l-Arabinose Isomerase from Enterococcus Faecium for d-Tagatose Synthesis.Molecules (Basel, Switzerland) · 2017Article
- Cloning, Expression, and Characterization of a Novel L-Arabinose Isomerase from the Psychrotolerant Bacterium Pseudoalteromonas haloplanktis.Molecular biotechnology · 2016Article
- Discovery, Molecular Mechanisms, and Industrial Applications of Cold-Active Enzymes.Frontiers in microbiology · 2016Review
- The secreted L-arabinose isomerase displays anti-hyperglycemic effects in mice.Microbial cell factories · 2015Article
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7 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
backgroundL-arabinose isomerases catalyse the isomerization of L-arabinose into L-ribulose at insight biological systems. At industrial scale of this enzyme is used for the bioconversion of D-galactose into D-tagatose which has many applications in pharmaceutical and agro-food industries. The isomerization reaction is thermodynamically equilibrated, and therefore the bioconversion rates is shifted towards tagatose when the temperature is increased. Moreover, to prevent secondary reactions it will be of interest to operate at low pH. The profitability of this D-tagatose production process is mainly related to the use of lactose as cheaper raw material. In many dairy products it will be interesting to produce D-tagatose during storage. This requires an efficient L-arabinose isomerase acting at low temperature and pH values.
resultsThe gene encoding the L-arabinose isomerase from Shewanella sp. ANA-3 was cloned and overexpressed in Escherichia coli. The purified protein has a tetrameric arrangement composed by four identical 55 kDa subunits. The biochemical characterization of this enzyme showed that it was distinguishable by its maximal activity at low temperatures comprised between 15-35°C. Interestingly, this biocatalyst preserves more than 85% of its activity in a broad range of temperatures from 4.0 to 45°C. Shewanella sp. ANA-3 L-arabinose isomerase was also optimally active at pH 5.5-6.5 and maintained over 80% of its activity at large pH values from 4.0 to 8.5. Furthermore, this enzyme exhibited a weak requirement for metallic ions for its activity evaluated at 0.6 mM Mn2+. Stability studies showed that this protein is highly stable mainly at low temperature and pH values. Remarkably, T268K mutation clearly enhances the enzyme stability at low pH values. Use of this L-arabinose isomerase for D-tagatose production allows the achievement of attractive bioconversion rates of 16% at 4°C and 34% at 35°C.
conclusionsHere we reported the purification and the biochemical characterization of the novel Shewanella sp. ANA-3 L-arabinose isomerase. Determination of the biochemical properties demonstrated that this enzyme was highly active at low temperatures. The generated T268K mutant displays an increase of the enzyme stability essentially at low pH. These features seem to be very attractive for the bioconversion of D-galactose into D-tagatose at low temperature which is very interesting from industrial point of view.
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